Regulation of expression of the p21CIP1 gene by the transcription factor ZNF217 and MDM2

被引：5

作者：

Mantsou, Aglaia ^{[1
]}

Koutsogiannouli, Evangelia ^{[1
,3
]}

Haitoglou, Costas ^{[1
]}

Papavassiliou, Athanasios G. ^{[2
]}

Papanikolaou, Nikolaos A. ^{[1
]}

机构：

[1] Aristotle Univ Thessaloniki, Biol Chem Lab, Div Biol Sci & Prevent Med, Fac Med, Univ Campus Bldg 16a, Thessaloniki 54124, Greece

[2] Univ Athens, Dept Biol Chem, Sch Med, 75 M Asias St, Athens 11527, Greece

[3] Heinrich Heine Univ, Dept Urol, Dusseldorf, Germany

来源：

BIOCHEMISTRY AND CELL BIOLOGY | 2016年 / 94卷 / 06期

关键词：

Affinity chromatography; MDM2; p21; promoter; ZNF217; RING-FINGER DOMAIN; HISTONE DEACETYLASES; UBIQUITIN LIGASE; P53; ACETYLATION; TERNARY COMPLEX; ACTIVATION; P53-MDM2; CELLS;

D O I：

10.1139/bcb-2016-0026

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

Using mouse double minute 2 (MDM2) protein-specific affinity chromatography and mass spectrometry, we have isolated the protein product of the oncogene znf217, which is a transcription factor and a component of a Hela-S-derived HDAC1 complex, as a novel MDM2-interacting protein. When co-expressed in cultured cancer cells, ZNF217 forms a complex with MDM2 and its ectopic over-expression reduces the steady-state levels of acetylated p53 in cell lines, suppressing its ability to activate the expression of a p21 promoter construct. In-silico analysis of the p21 promoter revealed the presence of several ZNF217-binding sites. These findings suggest that MDM2 controls p21 expression by at least 2 mechanisms: through ZNF217-mediated recruitment of HDAC1/MDM2 activity, which inhibits p53 acetylation; and through direct interaction with its binding site(s) on the p21 promoter.

引用

页码：560 / 568

页数：9

共 32 条

[31] CoREST is an integral component of the CoREST-human histone deacetylase complex [J].